1cc4
From Proteopedia
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| - | [[Image:1cc4.gif|left|200px]] | + | [[Image:1cc4.gif|left|200px]] |
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| - | '''PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.''' | + | {{Structure |
| + | |PDB= 1cc4 |SIZE=350|CAPTION= <scene name='initialview01'>1cc4</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=PHB:P-HYDROXYBENZOIC ACID'>PHB</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/4-hydroxybenzoate_3-monooxygenase 4-hydroxybenzoate 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.2 1.14.13.2] | ||
| + | |GENE= POBA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294 Pseudomonas fluorescens]) | ||
| + | }} | ||
| + | |||
| + | '''PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CC4 is a [ | + | 1CC4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CC4 OCA]. |
==Reference== | ==Reference== | ||
| - | Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability., Eppink MH, Bunthol C, Schreuder HA, van Berkel WJ, FEBS Lett. 1999 Jan 29;443(3):251-5. PMID:[http:// | + | Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability., Eppink MH, Bunthol C, Schreuder HA, van Berkel WJ, FEBS Lett. 1999 Jan 29;443(3):251-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10025942 10025942] |
[[Category: 4-hydroxybenzoate 3-monooxygenase]] | [[Category: 4-hydroxybenzoate 3-monooxygenase]] | ||
[[Category: Pseudomonas fluorescens]] | [[Category: Pseudomonas fluorescens]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:32 2008'' |
Revision as of 08:22, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | and | ||||||
| Gene: | POBA (Pseudomonas fluorescens) | ||||||
| Activity: | 4-hydroxybenzoate 3-monooxygenase, with EC number 1.14.13.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.
Overview
Phe161 and Arg166 of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens belong to a newly discovered sequence motif in flavoprotein hydroxylases with a putative dual function in FAD and NADPH binding [1]. To study their role in more detail, Phe161 and Arg166 were selectively changed by site-directed mutagenesis. F161A and F161G are catalytically competent enzymes having a rather poor affinity for NADPH. The catalytic properties of R166K are similar to those of the native enzyme. R166S and R166E show impaired NADPH binding and R166E has lost the ability to bind FAD. The crystal structure of substrate complexed F161A at 2.2 A is indistinguishable from the native enzyme, except for small changes at the site of mutation. The crystal structure of substrate complexed R166S at 2.0 A revealed that Arg166 is important for providing an intimate contact between the FAD binding domain and a long excursion of the substrate binding domain. It is proposed that this interaction is essential for structural stability and for the recognition of the pyrophosphate moiety of NADPH.
About this Structure
1CC4 is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.
Reference
Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability., Eppink MH, Bunthol C, Schreuder HA, van Berkel WJ, FEBS Lett. 1999 Jan 29;443(3):251-5. PMID:10025942
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